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1ORE

Human Adenine Phosphoribosyltransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0002055molecular_functionadenine binding
A0003999molecular_functionadenine phosphoribosyltransferase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006166biological_processpurine ribonucleoside salvage
A0006168biological_processadenine salvage
A0007625biological_processgrooming behavior
A0016208molecular_functionAMP binding
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0032263biological_processGMP salvage
A0032264biological_processIMP salvage
A0034774cellular_componentsecretory granule lumen
A0044209biological_processAMP salvage
A0046083biological_processadenine metabolic process
A0070062cellular_componentextracellular exosome
A1901363molecular_functionheterocyclic compound binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 2001
ChainResidue
ASER66
AARG67
AARG87
ALYS91

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE AMP A 1001
ChainResidue
AASP128
ALEU129
AALA131
ATHR132
AGLY133
AGLY134
ATHR135
ALEU159
AHOH2002
AHOH2024
AHOH2028
AHOH2070
AHOH2109
AVAL25
APHE26
AARG27
AARG67
AASP127

Functional Information from PROSITE/UniProt
site_idPS00103
Number of Residues13
DetailsPUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VVVVDDLLATGgT
ChainResidueDetails
AVAL123-THR135

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"12665801","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oro
ChainResidueDetails
ALYS91

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1oro
ChainResidueDetails
AGLU104
AARG67

243083

PDB entries from 2025-10-15

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